A0A0D3E188 · A0A0D3E188_BRAOL

Function

function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per monomer.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site31-36ATP (UniProtKB | ChEBI)
Binding site57a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site78-80a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site105-108a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site112CMP (UniProtKB | ChEBI)
Binding site144ATP (UniProtKB | ChEBI)
Binding site148a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site159a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site187ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionCMP kinase activity
Molecular FunctiondCMP kinase activity
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processpyrimidine nucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UMP-CMP kinase
  • EC number
  • Alternative names
    • Deoxycytidylate kinase
      (CK
      ; dCMP kinase
      )
    • Uridine monophosphate/cytidine monophosphate kinase
      (UMP/CMP kinase
      ; UMP/CMPK
      )

Organism names

  • Taxonomic identifier
  • Strain
    • cv. TO1000
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica

Accessions

  • Primary accession
    A0A0D3E188

Proteomes

Genome annotation databases

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    209
  • Mass (Da)
    23,321
  • Last updated
    2015-04-29 v1
  • MD5 Checksum
    A07DDEE60B8FBFAA724540F091F38985
MGSIVDASNKEVNGTASEKRPAVIFVLGGPGSGKGTQCAYIVEHFGYTHLSAGDLLRAEIKSGSENGTMIQNMIKEGKIVPSEVTIKLLQKAIQENGNDKFLIDGFPRNEENRAAFEKVTGIEPKFVLFFECPEEEMERRLLGRNQGREDDNIETIRKRFKVFLESSLPVIQYYEAKGKVRKIHAAKPIEDVFQEVKAVFSPEAEKVEA

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help